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Regulation of RCAN1 protein activity by Dyrk1A protein-mediated phosphorylation
Jung MS, Park JH, Ryu YS, Choi SH, Yoon SH, Kwen MY, Oh JY, Song WJ et al.. The Journal of biological chemistry, 2011-09-30
Topic: Brain proteins, microglia and lab models
Two genes on chromosome 21, namely dual specificity tyrosine phosphorylation-regulated kinase 1A (Dyrk1A) and regulator of calcineurin 1 (RCAN1), have been implicated in some of the phenotypic characteristics of Down syndrome, including the early onset of Alzheimer disease. Although a link between Dyrk1A and RCAN1 and the nuclear factor of activated T cells (NFAT) pathway has been reported, it remains unclear whether Dyrk1A directly interacts with RCAN1. In the present study, Dyrk1A is shown to directly interact with and phosphorylate RCAN1 at Ser(112) and Thr(192) residues. Dyrk1A-mediated phosphorylation of RCAN1 at Ser(112) primes the protein for the GSK3β-mediated phosphorylation of Ser(108). Phosphorylation of RCAN1 at Thr(192) by Dyrk1A enhances the ability of RCAN1 to inhibit the phosphatase activity of calcineurin (Caln), leading to reduced NFAT transcriptional activity and enhanced Tau phosphorylation. These effects are mediated by the enhanced binding of RCAN1 to Caln and its extended half-life caused by Dyrk1A-mediated phosphorylation. Furthermore, an increased expression of phospho-Thr(192)-RCAN1 was observed in the brains of transgenic mice overexpressing the Dyrk1A protein. These results suggest a direct link between Dyrk1A and RCAN1 in the Caln-NFAT signaling and Tau hyperphosphorylation pathways, supporting the notion that the synergistic interaction between the chromosome 21 genes RCAN1 and Dyrk1A is associated with a variety of pathological features associated with DS.
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APA 7th
Jung, M. S., Park, J. H., Ryu, Y. S., Choi, S. H., Yoon, S. H., Kwen, M. Y., et al. (2011). Regulation of RCAN1 protein activity by Dyrk1A protein-mediated phosphorylation. The Journal of biological chemistry. https://doi.org/10.1074/jbc.m111.253971
Vancouver
Jung MS, Park JH, Ryu YS, Choi SH, Yoon SH, Kwen MY, et al. Regulation of RCAN1 protein activity by Dyrk1A protein-mediated phosphorylation. The Journal of biological chemistry. 2011. doi:10.1074/jbc.m111.253971. PMID: 21965663.
BibTeX
@article{jung2011-21965663,
author = {Jung, M. S. and Park, J. H. and Ryu, Y. S. and Choi, S. H. and Yoon, S. H. and Kwen, M. Y. and Oh, J. Y. and Song, W. J. and others},
title = {{Regulation of RCAN1 protein activity by Dyrk1A protein-mediated phosphorylation}},
journal = {The Journal of biological chemistry},
year = {2011},
doi = {10.1074/jbc.m111.253971},
pmid = {21965663},
url = {https://doi.org/10.1074/jbc.m111.253971}
}
Built from the record alzhub holds for this paper, not looked up. Volume, issue and page numbers are not held in the record. The record's author list ends in “et al.”, so not every author is named. Check the citation against the original before you use it.
Key findings
- These results suggest a direct link between Dyrk1A and RCAN1 in the Caln-NFAT signaling and Tau hyperphosphorylation pathways, supporting the notion that the synergistic interaction between the chromosome 21 genes RCAN1 and Dyrk1A is associated with a variety of pathological features associated with DS.
Why it matters
In this laboratory study, Dyrk1A was shown to directly interact with and phosphorylate RCAN1, which enhanced RCAN1's ability to inhibit calcineurin and led to enhanced tau phosphorylation. The authors suggest a direct link between these two chromosome 21 genes in pathways associated with Down syndrome features including early onset Alzheimer's disease.
Study details
- Evidence strengthLow
How this study scored 38/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported, studied in people and randomized / blinded because the record does not state it.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (The Journal of biological chemistry) |
| Journal's citation record | 4 / 4 | Journal of Biological Chemistry: journal h-index 780 (OpenAlex, 2026-10-29) |
| Study design | 0 / 12 | No study design recorded — scores zero, not guessed (not stated in the record — scored 0) |
| Strength of evidence | 1 / 5 | Rated “low” in our summary |
| Peer-review validation | 10 / 10 | Peer-reviewed. Published as an article in a named peer-reviewed journal. |
| How recent | 1 / 5 | 2011 — within 20 year(s) of the newest study here |
| Sample size | 0 / 4 | Participant count not stated — scores zero (not stated in the record — scored 0) |
| Effect reported | 0 / 3 | No effect size reported — scores zero (not stated in the record — scored 0) |
| Studied in people | 0 / 3 | Not stated whether this was studied in people — scores zero (not stated in the record — scored 0) |
| Randomized / blinded | 0 / 2 | No randomization or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 4 / 7 | Cited 89 times (OpenAlex, 2026-10-10) |
| Citations per year | 2 / 5 | 5.2 citations a year over 17 year(s) since 2011 |
| Impact for its field and year | 3 / 6 | Cited 3.5× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 2 / 6 | Cited by 4 other studies in this library |
| Still being cited | 1 / 4 | Cited 11 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 1 / 4 | Last-listed author Sul‐Hee Chung: h-index 13 (OpenAlex, whole career) |
| Institution's track record | 0 / 3 | Inje University: institution h-index 300 (OpenAlex) |
| Multicenter collaboration | 0 / 3 | OpenAlex lists 1 institution(s) in 1 country — scores zero (affiliation lists can be incomplete) |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 21965663) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 38 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1074/jbc.m111.253971
- PubMed: 21965663
- Original source →
- Free full text: Journal of Biological Chemistry →
Full text: free to read — OpenAlex lists this copy as free to read: the link above (checked 6 Feb 1020).
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